This request is for the Voyager DE STR Biospectrometry Workstation (MALDI TOF mass spectrometer) to be part of the Biochemical Research Service Laboratory (BRSL) at the University of Kansas, serving the Division of Biological Sciences and the Departments of Medicinal Chemistry, Pharmaceutical Chemistry, Pharmacology and Toxicology. The BRSL is an established core facility with a continuous record of growth. In the last three years two new services were established: DNA sequencing and Fermentation. Both proved to be extremely successful. Lt year more than 30 faculty members from 11 different departments used BRSL's services. The primary need for MALDI TOF instrument originates from the growing demand for bio-mass spectrometric analysis for the purposes of protein identification, localization of post-translational modifications and de novo mass spectrometric sequencing. The requested instrument will be operated collaboratively by the directors of the BRSL and the Mass Spectrometry Laboratory (MSL) and their staff, to create an optimum synthesis of sample preparation and handling, instrument operation and maintenance, and the data output and analysis. While the BRSL sample preparation and handling, instrument operation and maintenance, and the data output and analysis. While the BRSL and the MSL are separate entities on paper, they are part of the same overall research support infrastructure and they interact among themselves as well as with individual investigators (clients to both labs) on a regular and frequent basis. Presently micro-characterization of proteins by the BRSL is conducted by an outdated ABI 477 (bought in 1987) with unacceptably poor sensitivity. The MSL's only instrument capable of handling large molecules of biological interest is an Autospec-Q (Tandem hybrid of EBEqQ geometry purchased in 1991 and equipped for electrospray ionization (ESI) in 1995). Time on the Autospec can be difficult to schedule, especially when HPLC/MS is being run. Further, experience has shown Time on the Autospec can be difficult to schedule, especially when HPLC/MS is being run. Further, experience has shown that ESI, while powerful, is simply not capable of solving all protein characterization problems. MALDI has been shown to be quite complementary in capability. MALDI TOF analysis is characterized by easier data interpretation from mixtures (fewer charge state concerns) and is more tolerant of detergents and salts. The availability of a MALDI TOF instrument in a core lab dedicated to biosamples, close to the investigators involved in sample isolation and purification, would greatly enhance our power to analyze important biological molecules.